Rat Pulmonary surfactant-associated protein A,SP-A ELISA Kit

Code CSB-E08684r
Size 96T,5×96T,10×96T
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Trial Size 24T ELISA Kit Trial Size (Only USD$150/ kit)
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Product Details

Alternative Names
Sftpa1 ELISA Kit; Sftp-1 ELISA Kit; Sftp1 ELISA Kit; Sftpa ELISA Kit; Pulmonary surfactant-associated protein A ELISA Kit; PSAP ELISA Kit; PSP-A ELISA Kit; SP-A ELISA Kit
Uniprot No.
Rattus norvegicus (Rat)
Sample Types
serum, plasma, tissue homogenates
Detection Range
31.25 pg/ml - 2000 pg/ml
7.8 pg/ml
Assay Time
Sample Volume
Detection Wavelength
450 nm
Research Area
Signal Transduction
Assay Principle
and FAQs
Store at 2-8°C. Please refer to protocol.
Lead Time
3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx

The Rat Pulmonary surfactant-associated protein A (SP-A) ELISA Kit is designed for precise and accurate measurement of SP-A protein levels in various sample types. The kit is developed to detect the Sftpa1 gene product, a vital component of the pulmonary surfactant complex, which is involved in respiratory function and immune regulation.

The kit is suitable for the analysis of serum, plasma, and tissue homogenates, making it a versatile tool for research in signal transduction. The detection range of the kit is 31.25 pg/ml - 2000 pg/ml with a sensitivity of 7.8 pg/ml, allowing for precise quantification of SP-A protein levels in a wide range of concentrations.

The assay time for this kit is 1-5 hours, and the sample volume required is 50-100ul. The detection wavelength is 450 nm, ensuring high sensitivity and specificity in sample analysis. Its superior quality, reproducibility, and specificity make it an excellent tool for researchers in signal transduction.

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Target Background

(From Uniprot)
In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages.
Gene References into Functions
  1. SP-A expression was up-regulated in the middle ear effusion of non-typeable Haemophilus influenza otitis media. PMID: 30055742
  2. SPA binds dipalmitoyl-phosphatidylcholine, the major surfactant lipid component, but not phosphatidylinositol; SPD exhibits the opposite preference. Data suggest flexibility in a key surface loop supports distinctive lipid binding of SPA; quadruple mutant SPA (E171D/P175E/R197N/K203D) that introduces SPD-like loop-stabilizing Ca2+ binding site in carbohydrate recognition domain exhibits ligand-binding preferences of SPD. PMID: 28719181
  3. Downregulation of SP-A expression caused due to silica is an important factor in the occurrence and development of silicosis. PMID: 27660222
  4. Liraglutide activates the GLP1 receptor, increasing ACE2 expression, reversing right ventricle hypertrophy, and improving the production of SP-A and SP-B in the lungs of Type 1 Diabetes rats PMID: 26196539
  5. Mutations of rat surfactant protein A have distinct effects on its glycosylation, secretion, aggregation and degradation. PMID: 25242514
  6. Dual positive effects of leptin were found on protein expression and transcriptional activity of thyroid transcription factor-1 PMID: 23894445
  7. VIP can up-regulate the expression of SP-A in alveolar type II cells. PMID: 21166190
  8. NG-nitro-L-arginine can protect the lung from LPS-induced injury by up-regulating the expression of PS. PMID: 20663300
  9. A novel role is demonstrated for SP-A in modulating endolysosomal trafficking via Rab7b (but not Rab5 nor Rab11) in primary alveolar macrophages, and the biochemical pathways are defined. PMID: 21248257
  10. SP-A stimulates the release of neutrophil chemotactic factor by alveolar type II cells, and this effect is mediated by the receptor for SP-A specifically expressed by these cells. PMID: 20473679
  11. VIP elevated SP-A expression in ATII cells which was mediated by enhanced sp-a gene transcription PMID: 20688121
  12. crystal structures of calcium-dependent complexes of the C-terminal neck and carbohydrate recognition domain of SP-A with carbohydrates PMID: 21047777
  13. The SPA level decreases significantly in acute pulmonary embolism. PMID: 16207426
  14. Data suggest that the pathway for secretion of newly synthesized surfactant protein-A is by transfer from the site of synthesis to the storage/secretory organelle prior to lamellar body exocytosis. PMID: 20382745
  15. the ability of SP-A to inhibit immune cell activation by Re-LPS may be due to its ability to block the binding of Re-LPS to LBP and prevent the initiation of the LBP/CD14 pathway for inflammatory reactions in the lung. PMID: 12204898
  16. SP-A selectively enhances mannose receptor expression on monocyte-derived macrophages, a process involving both the attached sugars and collagen-like domain of SP-A. PMID: 12244146
  17. SP-A can reverse the detrimental effects of surfactant oxidation on the biophysical properties of surfactant, by a mechanism that is dependent on interchain disulfide bond formation and the C-terminal domains of the protein. PMID: 12600986
  18. SP-A and SP-D are antimicrobial proteins that directly inhibit the growth of Histoplasma capsulatum by increasing permeability of the organism PMID: 12857753
  19. blocks secretagogue-stimulated phospholipid release, even in the presence of surfactant-like lipid PMID: 12882765
  20. Results suggest that there is no primary deficiency of surfactant proteins A, B, or C in the nitrofen-induced rat model of congenital diaphragmatic hernia. PMID: 12904592
  21. Crystal structure of trimeric carbohydrate recognition and neck domains of surfactant protein A PMID: 12913002
  22. SP-A enhances the phagocytosis of S. pneumoniae by alveolar macrophages through a CK2-dependent increase of cell surface SR-A localization (scavenger receptor a) PMID: 14993215
  23. SP-A and SP-D enhance mannose receptor-mediated phagocytosis of M. avium by macrophages PMID: 15187139
  24. Differential allele-specific expression was observed in all tissues studied (OPN) or in all extrapulmonary tissues (SP-A). Double heterozygous rats revealed lack of coordinate allele expression among SP-A, SP-D, and OPN. PMID: 15482851
  25. NO mediated the decrease in surfactant protein gene expression PMID: 15640287
  26. We suggest that enhanced release of surfactant phospholipids and SP-A represents an early protective response that compensates in part for the inactivation of intraalveolar surfactant in the early phase of IR injury. PMID: 15969762
  27. The addition of rat or recombinant rat SP-A to human monocyte-derived macrophages significantly raises the level of cytosolic calcium above baseline within 10 seconds of SP-A addition PMID: 16081790
  28. SP-A and Prdx6 directly interact, which provides a mechanism for regulation of the PLA(2) activity of Prdx6 by SP-A PMID: 16330552
  29. results indicated SP-A & SP-D have distinct functions in lung homeostasis & the function of the neck domain & carbohydrate recognition domain of SP-D is dependent on its own NH2-terminal & collagenous domains that cannot be complemented by those of SP-A PMID: 16500946
  30. Direct effect of SFTPA1 on rat myometrial cells and inhibitory cross talk between SFTPA1 and LPS signals. PMID: 17202387
  31. SP-A2 enhances phagocytosis of Pseudomonas aeruginosa by rat alveolar macrophages more than does SP-A1. PMID: 17220308
  32. Air spaces of neonatal lungs comprised lower fractions of tubular myelinand increased unilamellar vesicles, which correlated with low SP-A concentrations in lung lavage fluid and increased respiratory rates, respectively PMID: 17469149
  33. alterations of surfactant are a consequence of the ventilation strategy that impair the biophysical activity of this material and thereby contribute directly to lung dysfunction over time PMID: 18344412
  34. cigarette smoke alone decreases the level of SP-A and that might have an important effect on surfactant metabolism and the host defense functions of surfactant in the peripheral airways PMID: 18480979
  35. After OVA challenge alveolar epithelial cells Type II (AEII) show a significantly higher expression of SP-A and SP-D leading also to higher amounts of both SPs in BALF, and macrophages gather predominantly SP-A. PMID: 18802356

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Subcellular Location
Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Protein Families
SFTPA family
Database Links
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